5A48

Crystal structure of the LOTUS domain (aa 139-240) of Drosophila Oskar in P65

5A48 の概要

• エントリーDOI: 10.2210/pdb5a48/pdb
• 関連するPDBエントリー: 5A49 5A4A
• 分子名称: MATERNAL EFFECT PROTEIN OSKAR (2 entities in total)
• 機能のキーワード: protein binding, ost-hth domain, winged helix-turn-helix, dimer, vasa interaction, germ plasm
• 由来する生物種: DROSOPHILA MELANOGASTER (FRUIT FLY)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 23402.47

構造登録者

Jeske, M.,Glatt, S.,Ephrussi, A.,Mueller, C.W. (登録日: 2015-06-05, 公開日: 2015-07-22, 最終更新日: 2024-05-08)

主引用文献

Jeske, M.,Bordi, M.,Glatt, S.,Muller, S.,Rybin, V.,Muller, C.W.,Ephrussi, A.
The Crystal Structure of the Drosophila Germline Inducer Oskar Identifies Two Domains with Distinct Vasa Helicase-and RNA-Binding Activities.
Cell Rep., 12:587-, 2015

PubMed Abstract: In many animals, the germ plasm segregates germline from soma during early development. Oskar protein is known for its ability to induce germ plasm formation and germ cells in Drosophila. However, the molecular basis of germ plasm formation remains unclear. Here, we show that Oskar is an RNA-binding protein in vivo, crosslinking to nanos, polar granule component, and germ cell-less mRNAs, each of which has a role in germline formation. Furthermore, we present high-resolution crystal structures of the two Oskar domains. RNA-binding maps in vitro to the C-terminal domain, which shows structural similarity to SGNH hydrolases. The highly conserved N-terminal LOTUS domain forms dimers and mediates Oskar interaction with the germline-specific RNA helicase Vasa in vitro. Our findings suggest a dual function of Oskar in RNA and Vasa binding, providing molecular clues to its germ plasm function.

PubMed: 26190108
DOI: 10.1016/J.CELREP.2015.06.055

実験手法

X-RAY DIFFRACTION (2.35 Å)